Wakasa Yuhya, Takagi Hidenori, Watanabe Nobumasa, Kitamura Noriko, Fujiwara Yoshihiro, Ogo Yuko, Hayashi Shimpei, Yang Lijun, Ohta Masaru, Thet Tin Wai Wai, Sekikawa Kenji, Takano Makoto, Ozawa Kenjirou, Hiroi Takachika, Takaiwa Fumio
Genetically Modified Organism Research Center, National Institute of Agrobiological Sciences, Kannondai, Tsukuba, Ibaraki, Japan.
Department of Allergy and Immunology, Tokyo Metropolitan Institute of Medical Science, Kamikitazawa, Setagaya-ku, Tokyo, Japan.
PLoS One. 2015 Mar 16;10(3):e0120209. doi: 10.1371/journal.pone.0120209. eCollection 2015.
The endoplasmic reticulum-derived type-I protein body (PB-I) from rice endosperm cells is an ideal candidate formulation for the oral delivery of bioencapsulated peptides as tolerogens for allergen-specific immunotherapy. In the present study, PBs containing the deconstructed Japanese cedar pollen allergens Cryptomeria japonica 1 (Cry j 1) and Cry j 2 were concentrated by treatment with thermostable α-amylase at 90°C to remove the starch from milled rice powder, which resulted in a 12.5-fold reduction of dry weight compared to the starting material. The modified Cry j 1 and Cry j 2 antigens in this concentrated PB product were more resistant to enzymatic digestion than those in the milled seed powder despite the absence of intact cell wall and starch, and remained stable for at least 10 months at room temperature without detectable loss or degradation. The high resistance of these allergens could be attributed to changes in protein physicochemical properties induced by the high temperature concentration process, as suggested by the decreased solubility of the antigens and seed proteins in PBs in step-wise-extraction experiments. Confocal microscopy showed that the morphology of antigen-containing PB-Is was preserved in the concentrated PB product. The concentrated PB product induced specific immune tolerance against Cry j 1 and Cry j 2 in mice when orally administered, supporting its potential use as a novel oral tolerogen formulation.
来自水稻胚乳细胞的内质网衍生I型蛋白体(PB-I)是生物包封肽口服递送的理想候选制剂,可作为变应原特异性免疫疗法的耐受原。在本研究中,通过在90°C下用耐热α-淀粉酶处理,浓缩含有解构的日本柳杉花粉变应原日本柳杉1(Cry j 1)和Cry j 2的蛋白体,以去除米粉中的淀粉,与起始材料相比,干重减少了12.5倍。尽管没有完整的细胞壁和淀粉,但该浓缩PB产品中的修饰Cry j 1和Cry j 2抗原比磨碎的种子粉中的抗原更耐酶消化,并且在室温下至少保持稳定10个月,没有可检测到的损失或降解。如逐步提取实验中PBs中抗原和种子蛋白溶解度降低所示,这些变应原的高抗性可能归因于高温浓缩过程引起的蛋白质物理化学性质的变化。共聚焦显微镜显示,浓缩PB产品中保留了含抗原的PB-I的形态。当口服给药时,浓缩PB产品在小鼠中诱导了针对Cry j 1和Cry j 2的特异性免疫耐受,支持其作为新型口服耐受原制剂的潜在用途。